Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy.

@article{Nanga2009ThreedimensionalSA,
  title={Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy.},
  author={Ravi Prakash Nanga and Jeffrey R. Brender and Jiadi Xu and Kevin Hartman and Vivekanandan Subramanian and Ayyalusamy Ramamoorthy},
  journal={Journal of the American Chemical Society},
  year={2009},
  volume={131 23},
  pages={8252-61}
}
Islet amyloid polypeptide (IAPP or amylin) is a 37-residue peptide hormone associated with glucose metabolism that is cosecreted with insulin by beta-cells in the pancreas. Since human IAPP is a highly amyloidogenic peptide, it has been suggested that the formation of IAPP amyloid fibers is responsible for the death of beta-cells during the early stages of type II diabetes. It has been hypothesized that transient membrane-bound alpha-helical structures of human IAPP are precursors to the… CONTINUE READING
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